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Information on EC 1.2.1.30 - carboxylate reductase (NADP+) and Organism(s) Nocardia iowensis and UniProt Accession Q6RKB1
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1.2.1.30 carboxylate reductase (NADP+)IUBMB Comments
The enzyme contains an adenylation domain, a phosphopantetheinyl binding domain, and a reductase domain, and requires activation by attachment of a phosphopantetheinyl group. The enzyme activates its substrate to an adenylate form, followed by a transfer to the phosphopantetheinyl binding domain. The resulting thioester is subsequently transferred to the reductase domain, where it is reduced to an aldehyde and released.
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Word Map
- 1.2.1.30
- synthesis
-
bio-based
-
fragrance
-
autoinduction
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phosphopantetheinylation
-
over-reduction
- benzaldehyde
- industry
The taxonomic range for the selected organisms is: Nocardia iowensis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
carboxylate reductases, nicar, macar, nocar, nccar, mmcar, aryl-aldehyde oxidoreductase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aromatic acid reductase
-
-
-
-
aryl-aldehyde dehydrogenase (NADP+)
-
-
-
-
CAR
Carboxylic acid reductase
niCAR
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
carboxylic acid and ATP are first bound in the A-domain, wherein the alpha-phosphate of ATP is attacked by the acid, releasing pyrophosphate and forming an acyl-adenylate complex. The CAR enzyme then undergoes a domain shift into a thiolation state where the adenylate is then attacked by the thiol group on the phosphopantetheine arm at the carbonyl carbon, forming a thioester and releasing AMP. The CAR enzyme then undergoes another domain shift where the phosphopantetheine arm is exposed in the R-domain. Finally, the thioester is reduced by NADPH, producing the aldehyde product while returning the phosphopantetheine arm to its thiol form
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
product inhibition by NADP+, adenosine monophosphate, and diphosphate indicates that the binding of substrates at the adenylation domain is ordered with ATP binding first, proposed catalytic mechanism in 4 steps, overview. The first two steps, the relatively unreactive carboxylic acid is activated to form a thioester with the phosphopantetheine arm at the N-terminal adenylation domain (1) ATP and a carboxylic acid enter the active site of the adenylation domain in which the alpha-phosphate of ATP is attacked by an O atom from the carboxylic acid to form an AMP-acyl phosphoester with the release of diphosphate.(2) The thiol group of the phosphopantetheine arm can then attack the carbonyl carbon atom of the AMP-acyl phosphoester intermediate nucleophilically to release AMP and to form an acyl thioester with the phosphopantetheine arm. (3) The phosphopantetheine arm transfers to the C-terminal reductase domain in which (4) the thioester is reduced by NADPH, the aldehyde and NADP+ are released, and the thiol of the phosphopantetheine arm is regenerated in the process
an aromatic aldehyde + NADP+ + AMP + diphosphate = an aromatic acid + NADPH + H+ + ATP
the catalytic cycle starts with the activation of the carboxylate substrate with ATP in the A-domain, yielding an AMP-ester intermediate under release of pyrophosphate as the co-product. The active thiol tether of the phosphopantetheinyl moiety then binds the carboxylate, releasing AMP as a leaving group. The resulting thioester is subsequently transferred to the R domain, where it is reduced to the corresponding aldehyde product. The aldehyde is not amenable to enter a second catalytic cycle. The enzyme does not catalyze the overreduction of the aldehyde product to the respective alcohol
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
aryl-aldehyde:NADP+ oxidoreductase (ATP-forming)
The enzyme contains an adenylation domain, a phosphopantetheinyl binding domain, and a reductase domain, and requires activation by attachment of a phosphopantetheinyl group. The enzyme activates its substrate to an adenylate form, followed by a transfer to the phosphopantetheinyl binding domain. The resulting thioester is subsequently transferred to the reductase domain, where it is reduced to an aldehyde and released.
CAS REGISTRY NUMBER
COMMENTARY
9074-94-6
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(E)-3-phenylprop-2-enoate + NADPH + H+ + ATP
(E)-3-phenylprop-2-enal + NADP+ + AMP + diphosphate
-
-
-
?
3-hydroxypropionate + NADPH + H+ + ATP
3-hydroxypropanal + NADP+ + AMP + diphosphate
-
-
-
-
ir
3-methoxybenzoate + NADPH + H+ + ATP
3-methoxybenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
3-nitrobenzoate + NADPH + H+ + ATP
3-nitrobenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
3-oxo-3-phenylpropanoate + NADPH + H+ + ATP
3-oxo-3-phenylpropanal + NADP+ + AMP + diphosphate
-
-
-
?
3-phenylprop-2-ynoate + NADPH + H+ + ATP
3-phenylprop-2-ynal + NADP+ + AMP + diphosphate
-
-
-
?
3-phenylpropionate + NADPH + H+ + ATP
3-phenylpropionaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
4-hydroxybutyrate + NADPH + H+ + ATP
4-hydroxybutanal + NADP+ + AMP + diphosphate
-
-
-
-
ir
4-methoxybenzoate + NADPH + H+ + ATP
4-methoxybenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
4-methylbenzoate + NADPH + H+ + ATP
4-methylbenzaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
5-hydroxypentanoate + NADPH + H+ + ATP
5-hydroxypentanal + NADP+ + AMP + diphosphate
-
-
-
-
ir
alpha-ketoglutaric acid + NADPH + ATP
? + NADP+ + AMP + phosphate
-
-
-
?
aromatic acid + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
?
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
benzoic acid + NADPH + H+ + ATP
benzaldehyde + benzyl alcohol + NADP+ + AMP + diphosphate
-
-
-
?
butanoate + NADPH + H+ + ATP
butyraldehyde + NADP+ + AMP + diphosphate
-
-
-
?
dodecanoate + NADPH + H+ + ATP
dodecanal + NADP+ + AMP + diphosphate
-
-
-
?
ferulic acid + NADPH + H+ + ATP
ferulic acid + coniferyl aldehyde + coniferyl alcohol + NADP+ + AMP + diphosphate
not completely reduced
-
-
?
glutarate + NADPH + H+ + ATP
5-oxopentanoate + 1,5-pentanedial + NADP+ + AMP + diphosphate
-
-
-
-
ir
malonate + NADPH + H+ + ATP
3-oxopropanoate + 1,3-propanedial + NADP+ + AMP + diphosphate
-
low activity
-
-
ir
octadecanoate + NADPH + H+ + ATP
octadecanal + NADP+ + AMP + diphosphate
-
-
-
?
octanoate + NADPH + H+ + ATP
octanal + NADP+ + AMP + diphosphate
-
-
-
?
succinate + NADPH + H+ + ATP
4-oxobutanoate + 1,4-butanedial + NADP+ + AMP + diphosphate
-
-
-
-
ir
thiophene-2-carboxylate + NADPH + H+ + ATP
thiophene-2-carbaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
trans-2-phenylcyclopropane-1-carboxylate + NADPH + H+ + ATP
trans-2-phenylcyclopropane-1-carbaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
trans-aconitic acid + NADPH + ATP
? + NADP+ + AMP + phosphate
-
-
-
?
vanillate + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
-
-
-
-
ir
vanillic acid + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
-
-
-
?
vanillic acid + NADPH + H+ + ATP
vanillin + vanillyl alcohol + NADP+ + AMP + diphosphate
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with Escherichia coli BL21-CodonPlus(DE3)-RP/pPV2.83, in which recombinant Npt is expressed along with recombinant car, vanillic acid is reduced to vanillin and vanillyl alcohol, with vanillin (80%) as the major product. Escherichia coli BL21-CodonPlus(DE3)-RP/pHAT305 (expressing only recombinant Car) reduce only 50% of the vanillic acid starting material, with vanillyl alcohol being the major metabolite. With Escherichia coli BL21-CodonPlus(DE3)-RP/pPV2.83, in which recombinant car is presumed to be in the fully active, phosphopantetheinylated holo form, the rate of reduction of vanillic acid is much faster than that of vanillin to vanillyl alcohol by endogenous Escherichia coli aldehyde dehydrogenase
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-
?
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
?
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
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ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
via an adenylated intermediate
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-
ir
additional information
?
-
pyruvic, isocitric acid, fumaric acid and maleic acid are not substrates for the enzyme
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-
?
additional information
?
-
CAR enzymes exhibit a broad substrate tolerance for the conversion of organic acids to the respective aldehydes
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-
-
additional information
?
-
carboxylic acid reductases (CARs) catalyze the two-electron reduction of carboxylic acids to aldehydes. The substrate scope of CARs is broad, encompassing a wide range of aromatic and aliphatic substrates
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-
-
additional information
?
-
no activity with 2-methoxybenzoate, 4-nitrobenzoate, 2-nitrobenzoate, pyridine-2-carboxylate, 1H-pyrrole-2-carboxylate, and furan-2-carboxylate
-
-
-
additional information
?
-
-
substrate specificity of recombinant hybrid mutant enzymes, overview
-
-
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
aromatic carboxylate + NADPH + H+ + ATP
aromatic aldehyde + NADP+ + AMP + diphosphate
-
-
-
ir
vanillate + NADPH + H+ + ATP
vanillin + NADP+ + AMP + diphosphate
-
-
-
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ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
-
-
-
-
ir
benzoate + NADPH + H+ + ATP
benzaldehyde + NADP+ + AMP + diphosphate
via an adenylated intermediate
-
-
ir
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phosphopantetheine transferase
-
required for activating the enzyme. Recombinant car is an apoenzyme that requires phosphopantetheinylation for conversion to a fully active holoenzyme
-
additional information
levels of recombinant Car and Gdh are slightly higher when cultures are grown without chloramphenicol
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additional information
for activation, CARs require PPTase-mediated posttranslational modification of the T-domain. Through the activity of PPTase, a phosphopantetheine arm is covalently bound to a highly conserved serine domain in the T-domain. The flexibility and length of this phosphopantetheine arm enables this activated residue to transition between the A- and R-domain active sites
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
stopped-flow measurements, steady-state (kcat) and single-turnover (kobs) kinetics of wild-type and hybrid mutant enzymes, comparisons, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.36
recombinant Car expressed in Escherichia coli BL21-CodonPlus(DE3)-RP cells cultured in LB medium with ampicillin, at 16 h
1.5
-
recombinant car incubated with CoA and Escherichia coli MV1190/pUC8-sfp cell free extract
1.6
-
Nocardia cell free extract incubated with recombinant car and CoA. Recombinant car incubated with CoA and Npt
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
lack of posttranslational phosphopantetheinylation of a serine group in the recombinant CAR reduces the activity of recombinantly expressed enzyme
physiological function
additional information
evolution
Aerobic bacteria and fungi typically express ATP- and NADPH-dependent enzymes, which were initially named aryl-aldehyde dehydrogenases (NADP+), but are meanwhile also mostly referred to as carboxylate reductases (CARs). These enzymes are classified as the EC 1.2.1.30 family. CAR sequences of the EC 1.2.1.30 family fall into four distinct subgroups
physiological function
-
carboxylic acid reductases (CARs) are valuable biocatalysts due to their ability to reduce a broad range of carboxylate substrates into the corresponding aldehyde products. CARs are multi-domain enzymes with separate catalytic domains for the adenylation and the subsequent reduction of substrates. Inter-domain dynamics are crucial for the catalytic activities of CARs
physiological function
CARs, or aryl-aldehyde oxidoreductases, are Mg2+-dependent multi-domain enzymes that irreversibly catalyze the reduction of carboxylic acids to aldehydes at the cost of one ATP and one NADPH. CARs have a broad substrate scope, encompassing a wide range of aromatic and aliphatic carboxylic acids. The purified enzyme from Nocardia iowensis reduces a broader range of substituted aromatic acids in addition to dicarboxylic acids of the citric acid cycle, resulting in a branding of the aryl-aldehyde oxidoreductase class more broadly as carboxylic acid reductases (CARs)
physiological function
requirement for the presence of a phosphopantetheine transferase for the loading of a phosphopantetheine group onto the CAR enzyme is shown for niCAR. Enzyme CAR prefers substrates in which the carboxylic acid is the only polar or charged group, which gives a useful insight into the substrate specificity of the enzymes. Model development for the prediction of CAR reactivity
physiological function
the phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
additional information
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively. Identification of key residues for CAR activity
additional information
structure-function analysis and structure comparisons
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the carboxylate reductase three-domain architecture is modular. CARs are comprised of three domains: an adenylation domain (A-domain), a phosphopantetheinyl binding domain (also called transthiolation domain (T-domain), or peptidyl carrier protein (PCP domain)), and a reductase domain (R-domain). The phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine
additional information
the structure of CARs is characterized through three functional domains: an N-terminal adenylation domain (A-domain), a thiolation or peptidyl carrier protein domain (T-domain), and a C-terminal reduction domain (R-domain). Structure comparisons, overview. The A-domains of CARs are members of the ANL superfamily of adenylating enzymes. The T-domain is between 80 and 120 residues in length and is highly dynamic in nature, due to the flexible linker regions connecting the alpha helix bundle to neighboring domains in NRPSs and CARs. Domain crystal structures of CARs have demonstrated the dynamic nature of the T-domain, with the activated phosphopantetheinyl-serine positioned away from A-domains in the adenylation state (ATP bound) and situated between 20-50 A from A-domains in the thiolation state (AMP bound). While the T-domain is flexible, its short amino acid length and current domain crystal structures indicate that domain shifts involve dynamic rearrangement in both the A- and R-domains as well. Reduction domain structure and activity, molecular dynamics (MD) study
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphopantetheinylation
posttranslational phosphopantetheinylation of a serine group in the recombinant CAR that is necessary for activity
side-chain modification
The phosphopantetheinyl-binding domain is recognized by a phosphopantetheinyl transferase enzyme, which attaches a phosphopantetheinyl residue to a conserved serine. Only upon this post-translational modification, the enzymes become active and are able to engage in the catalytic cycle
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
analysis of A-T-R domain architecture with relaxed substrate specificity, structure-function-relationship and potential as biocatalysts for organic synthesis, respectively
additional information
-
hybrid enzymes that contain domains from four bacterial CARs and one fungal CAR are constructed based on domain boundaries that are defined using a combination of bioinformatics and structural analysis. Hybrid CARs are characterized in both steady-state and transient kinetics studies using aromatic and straight-chain (C3-C5) carboxylate substrates. Kinetic data support that the inter-domain interactions play an important role in the function of both wild-type and hybrid CARs and further lead to the hypothesis that reduction is the rate-determining step in CAR catalysis. Analysis of CAR catalysis and rationale for hybrid CAR engineering, overview. Combination of Mycobacterium avium domains with domains (R, A, and P) from CARs derived from Nocardia iowensis (Ni) resulting in hybrid enzymes: Mav(A)-Ni(PR), Mav(AP)-Ni(R), Ni(A)-Mav(PR), and Ni(AP)-Mav(R), kinetic analysis with dicarboxylate and hydroxyacid substrates, domain dynamics of hybrid CARs. Analysis of substrate specificity of recombinant hybrid mutant enzymes
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
enzyme half-lives at different conditions, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography and desalting gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, phylogenetic analysis
DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli resulting in decreased activity due to a lack of post-translational phosphopantetheinylation of a serine group in the recombinant CAR that is necessary for activity. Coexpression with the recombinant phosphopantetheinyl transferase (PPTase) from Bacillus subtilis (Sfp) or cell-free extracts from Nocardia iowensis containing native PPTase converted niCAR to its holoenzyme state, increases the enzyme activity 20fold. Recombinant enzyme expression in Saccharomyces cerevisiae and Saccharomyces pombe and an engineered aldehyde-accumulating Escherichia coli strain for de novo production of vanillin from glucose
plasmids pHAT305(Placcar), pPV2.83(Placcar Placnpt), pPV2.84(Placcar Placgdh) or pPV2.85(Placcar Plac npt gdh) expressed in Escherichia coli BL21-CodonPlus(DE3)-RP cells
recombinant car expressed in Escherichia coli BL21-CodonPlus(DE3)-RP/pHAT305 and in Escherichia coli BL21-CodonPlus(DE3)-RP/pPV1.184 cells
-
sequence comparisons and phylogenetic analysis, recombinant coexpression of His-tagged enzyme in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
industry
vanillic acid reduction in Escherichia coli BL21-CodonPlus(DE3)-RP/pPV2.85 cells containing car, npt and gdh is complete in 6 h, and is faster than in cells containing only car and/or npt. The availability of Escherichia coli BL21-CodonPlus(DE3)-RP/pPV2.85 expressing holo-Car and Gdh provides a means of generating a range of value-added aldehydes or alcohols of importance in pharmaceutical, food and agricultural industries. Uses of directed evolution and related mutant generating processes, may enable a Car-system with broader substrate specificities and one that is capable of achieving much higher product yields
synthesis
synthesis
carboxylic acid reductases (CARs) catalyze the conversion of carboxylic acids to aldehydes, which are a valuable class of chemicals for many consumer and industrial applications. CARs generally exhibit broad substrate specificity that encompasses aromatic, aliphatic, and di/tri-carboxylic acids, enabling the development of biosynthetic pathways to a wide array of potential aldehyde products. De novo biosynthesis utilizing CARs have produced industrially relevant products including aromatic aldehydes, fatty and aromatic alcohols, and alkanes. De novo synthetic pathways implementing CARs have enabled the production of sustainable aldehyde products or utilized highly reactive aldehydes as intermediates in the production of chemicals including amines, alcohols, and alkanes. Aromatic aldehydes, such as vanillin, benzaldehyde, and cinnamaldehyde are particularly valuable in the fragrance and flavoring industries and are produced from petroleum feedstocks in large quantities. Recombinant enzyme expression in Saccharomyces cerevisiae and Saccharomyces pombe and an engineered aldehyde-accumulating Escherichia coli strain for de novo production of vanillin from glucose. Aldehydes as reactive intermediates in biosynthetic pathways, overview
synthesis
carboxylic acid reductases are important enzymes in the toolbox for sustainable chemistry and provide specific use as biocatalysts. The reduction of racemic ibuprofen by whole Nocardia iowensis cells gives an enantiomeric excess (ee) of 61.2%, which is attributed to enantioselectivity by niCAR based on kinetic data for its reduction of (S)-(+)- and (R)-(-)-ibuprofen enantiomers
synthesis
the enzyme can be useful for aromatic aldehyde synthesis on industrial level. The product selectivity is an essential asset of the enzyme if it is used for the biocatalytic synthesis of organic molecules on the preparative level
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Venkitasubramanian, P.; Daniels, L.; Das, S.; Lamm, A.S.; Rosazza, J.P.
Aldehyde oxidoreductase as a biocatalyst: Reductions of vanillic acid
Enzyme Microb. Technol.
42
130-137
2008
Nocardia iowensis (Q6RKB1)
Venkitasubramanian, P.; Daniels, L.; Rosazza, J.P.
Reduction of carboxylic acids by Nocardia aldehyde oxidoreductase requires a phosphopantetheinylated enzyme
J. Biol. Chem.
282
478-485
2007
Nocardia iowensis
Finnigan, W.; Thomas, A.; Cromar, H.; Gough, B.; Snajdrova, R.; Adams, J.P.; Littlechild, J.A.; Harmer, N.J.
Characterization of carboxylic acid reductases as enzymes in the toolbox for synthetic chemistry
ChemCatChem
9
1005-1017
2017
Mycobacterium marinum (B2HN69), Mycobacterium marinum ATCC BAA-535 (B2HN69), Mycolicibacterium phlei, Mycolicibacterium smegmatis, Neurospora crassa, Nocardia asteroides, Nocardia asteroides JCM 3016, Nocardia brasiliensis, Nocardia iowensis (Q6RKB1), Nocardia otitidiscaviarum, Syncephalastrum racemosum, Trametes versicolor, Tsukamurella paurometabola
Stolterfoht, H.; Schwendenwein, D.; Sensen, C.W.; Rudroff, F.; Winkler, M.
Four distinct types of E.C. 1.2.1.30 enzymes can catalyze the reduction of carboxylic acids to aldehydes
J. Biotechnol.
257
222-232
2017
Aspergillus terreus (Q0CRQ4), Aspergillus terreus FGSC A1156 (Q0CRQ4), Aspergillus terreus NIH 2624 (Q0CRQ4), Mycobacterium marinum (B2HN69), Mycobacterium marinum ATCC BAA-535 (B2HN69), Neurospora crassa, Nocardia iowensis (Q6RKB1), Segniliparus rotundus (D6Z860), Segniliparus rotundus ATCC BAA-972 (D6Z860), Segniliparus rotundus CDC 1076 (D6Z860), Segniliparus rotundus CIP 108378 (D6Z860), Segniliparus rotundus DSM 44985 (D6Z860), Segniliparus rotundus JCM 13578 (D6Z860)
Kramer, L.; Le, X.; Hankore, E.D.; Wilson, M.A.; Guo, J.; Niu, W.
Engineering and characterization of hybrid carboxylic acid reductases
J. Biotechnol.
304
52-56
2019
Kutzneria albida, Mycobacterium avium, Mycobacterium marinum (B2HN69), Mycobacterium marinum ATCC BAA-535 (B2HN69), Neurospora crassa, Nocardia iowensis
Butler, N.; Kunjapur, A.M.
Carboxylic acid reductases in etabolic engineering
J. Biotechnol.
307
1-14
2020
Aspergillus niger, Moorella thermoacetica, Mycobacterium marinum (B2HN69), Mycobacterium marinum ATCC BAA-535 (B2HN69), Mycobacteroides abscessus, Neurospora crassa, Nocardia asteroides, Nocardia iowensis (Q6RKB1), Trametes versicolor
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